3VG0
Antibody Fab fragment
Summary for 3VG0
| Entry DOI | 10.2210/pdb3vg0/pdb |
| Related | 3v6o |
| Descriptor | Monoclonal antibody 9F8 Fab fragment L chain, Monoclonal antibody 9F8 Fab fragment H chain, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | antibody fab fragment, immunoglobulin fold, n-linked glycosylation site, fab fragment, lbd domain of obr receptor, immune system |
| Biological source | Mus musculus More |
| Total number of polymer chains | 2 |
| Total formula weight | 48406.72 |
| Authors | Carpenter, B.,Hemsworth, G.R.,Ross, R.J.,Artymiuk, P.J. (deposition date: 2012-01-10, release date: 2012-03-14, Last modification date: 2024-11-20) |
| Primary citation | Carpenter, B.,Hemsworth, G.R.,Wu, Z.,Maamra, M.,Strasburger, C.J.,Ross, R.J.,Artymiuk, P.J. Structure of the human obesity receptor leptin-binding domain reveals the mechanism of leptin antagonism by a monoclonal antibody. Structure, 20:487-497, 2012 Cited by PubMed Abstract: Leptin regulates energy homeostasis, fertility, and the immune system, making it an important drug target. However, due to a complete lack of structural data for the obesity receptor (ObR), leptin's mechanism of receptor activation remains poorly understood. We have crystallized the Fab fragment of a leptin-blocking monoclonal antibody (9F8), both in its uncomplexed state and bound to the leptin-binding domain (LBD) of human ObR. We describe the structure of the LBD-9F8 Fab complex and the conformational changes in 9F8 associated with LBD binding. A molecular model of the putative leptin-LBD complex reveals that 9F8 Fab blocks leptin binding through only a small (10%) overlap in their binding sites, and that leptin binding is likely to involve an induced fit mechanism. This crystal structure of the leptin-binding domain of the obesity receptor will facilitate the design of therapeutics to modulate leptin signaling. PubMed: 22405007DOI: 10.1016/j.str.2012.01.019 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.27 Å) |
Structure validation
Download full validation report
